Surface activity properties of cysteine-substituted C-terminal melittin analogues.
In order to extend our knowledge of factors important in the surface activity of melittin, cysteine was substituted for lysine-21 and lysine-21/glutamine-25 in a pair of synthetic peptide analogues. The first of these changes resulted in only modest effects on secondary structure (determined in 50% trifluoroethanol), emulsification and surface tension properties. Introduction of a second cysteine greatly reduced both the rate of surface tension decay and the equilibrium surface tension attained, although secondary structure (determined in 50% trifluoroethanol) was only slightly affected by this modification. This latter peptide completely lacked emulsification and haemolytic properties and was found to oligomerise readily due to the formation of intermolecular, disulphide bridges. These results indicate that oligomerisation abolishes surface activity in melittin.
Ebeling
S C
SC
Department of Biochemistry, University College Cork, Mardyke, Ireland.
Kelly
S M
SM
O'Kennedy
B T
BT
Price
N C
NC
Sheehan
D
D
D000818:Animals; D002942:Circular Dichroism; D003545:Cysteine / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004655:Emulsions; D006461:Hemolysis; D008555:Melitten / Q000031:analogs & derivatives*; D017433:Protein Structure, Secondary; D012756:Sheep; D013329:Structure-Activity Relationship; D013500:Surface Tension
D004655:Emulsions; D008555:Melitten; D003545:Cysteine